Antiport process

The gradients of H, Na, and other cations and anions established by ATPases and other energy sources can be used for secondary active transport of various substrates. The best-understood systems use Na or gradients to transport amino acids and sugars in certain cells. Many of these systems operate as symports, with the ion and the transported amino acid or sugar moving in the same direction (that is, into the cell). In antiport processes, the ion and the other transported species move in opposite directions. (For example, the anion transporter of erythrocytes is an antiport.) Proton symport proteins are used by E. coU and other bacteria to accumulate lactose, arabinose, ribose, and a variety of amino acids. E. coli also possesses Na -symport systems for melibiose as well as for glutamate and other amino acids. 

A similarly charged ion is transported simnltaneously but in the opposite direction (known as an antiport process). 

Simple lipophilic cations, like ammonium ions bearing long hydrocarbon chains, allow anion extraction into an organic phase and render liquid membranes permeable to anions by an anion exchange (antiport) process. Such carriers effect, for instance, selective transport of amino acid carboxylates [6.3] against inorganic anions like chloride. 

Fig. 4. Ion-driven cotransport mechanisms, (a) Symport process involving a symporter (e.g. Na+/glucose transporter) (b) antiport process involving an antiporter (e.g. erythrocyte band 3 anion transporter).

Active transport processes in cellular membranes are well understood in terms of Mitchell s chemiosmotic theory. The idea that, directly or indirectly, active transport is energized by the electrochemical gradient of protons which is generated by H -ATPase, and that the solute molecules are taken up by symport and antiport processes with as the working ion, has been fully confirmed in the case of plant cells as well. The electrochemical gradient of which, divided by the Faraday con-... 

Figure 1. Solute transfer across an idealised eukaryote epithelium. The solute must move from the bulk solution (e.g. the external environment, or a body fluid) into an unstirred layer comprising water/mucus secretions, prior to binding to membrane-spanning carrier proteins (and the glycocalyx) which enable solute import. Solutes may then move across the cell by diffusion, or via specific cytosolic carriers, prior to export from the cell. Thus the overall process involves 1. Adsorption 2. Import 3. Solute transfer 4. Export. Some electrolytes may move between the cells (paracellular) by diffusion. The driving force for transport is often an energy-requiring pump (primary transport) located on the basolateral or serosal membrane (blood side), such as an ATPase. Outward electrochemical gradients for other solutes (X+) may drive import of the required solute (M+, metal ion) at the mucosal membrane by an antiporter (AP). Alternatively, the movement of X+ down its electrochemical gradient could enable M+ transport in the same direction across the membrane on a symporter (SP). A, diffusive anion such as chloride. Kl-6 refers to the equilibrium constants for each step in the metal transfer process, Kn indicates that there may be more than one intracellular compartment involved in storage. See the text for details...

Antiporter, a secondary ion transporter that moves a solute against its electrochemical gradient by using energy derived from the movement of another solute in the opposite direction down its electrochemical gradient. Antiporters are also called exchangers, and the exchange process is sometimes referred to as counter transport. 

Methods of traversing the basolateral membrane include uptake systems for organic cations and anions via fadhtated diffusion and/or active transport [1]. Organic anions and cations cross the basolateral membrane via ATP-driven or secondary active processes (H -antiport) [2]. Basolateral uptake processes include the gamma-glutamyl transport system [3] and those for glycoproteins [4]. Certain proteins (insulin, epidermal growth factor (EGF)) are transcytosed across the tubular cells from the blood to the tubular lumen via receptor-mediated uptake [5]. 

The tricarboxylic acid cycle not only takes up acetyl CoA from fatty acid degradation, but also supplies the material for the biosynthesis of fatty acids and isoprenoids. Acetyl CoA, which is formed in the matrix space of mitochondria by pyruvate dehydrogenase (see p. 134), is not capable of passing through the inner mitochondrial membrane. The acetyl residue is therefore condensed with oxaloacetate by mitochondrial citrate synthase to form citrate. This then leaves the mitochondria by antiport with malate (right see p. 212). In the cytoplasm, it is cleaved again by ATP-dependent citrate lyase [4] into acetyl-CoA and oxaloacetate. The oxaloacetate formed is reduced by a cytoplasmic malate dehydrogenase to malate [2], which then returns to the mitochondrion via the antiport already mentioned. Alternatively, the malate can be oxidized by malic enzyme" [5], with decarboxylation, to pyruvate. The NADPH+H formed in this process is also used for fatty acid biosynthesis. 

Because of its cyclic nature, this process presents analogies with molecular catalysis it may be considered as physical catalysis operating a change in location, a translocation, on the substrate, like chemical catalysis operates a transformation into products. The carrier is the transport catalyst which strongly increases the rate of passage of the substrate with respect to free diffusion and shows enzyme-like features (saturation kinetics, competition and inhibition phenomena, etc.). The active species is the carrier-substrate supermolecule. The transport of substrate Sj may be coupled to the flow of a second species S2 in the same (symport) or opposite antiport) direction. 

As a final example, it should be noted that in the presence of valinomycin, K+ is taken up by mitochondria to compensate for the H+ lost in forming the proton gradient. This work confirms the ratio of four K+ taken up per pair of electrons passing the energy-conserving site and so is equivalent to the H+/site ratio.85 The protein responsible for K+/H+ antiport has been identified.86 Other potassium transport processes have been described.87... 

The site of nitrate reduction is on the inner side of the cytoplasmic membrane, even though the enzyme itself spans the membrane. This requires the presence of a transport process for nitrate. An electroneutral nitrate/nitrite antiporter seems a reasonable proposal, and has been described... 

Figure 2. Bulk calcium transport by the osteoclast. Net acid transport is driven by the vacuolar-type H+-ATPase with a specialized large membrane subunit. Transport is balanced by chloride transport, probably involving both a chloride channel (CLIC-5) and a chloride bicarbonate antiporter (CLCN7). Supporting transport processes include chloride-bicarbonate exchange. Insertion of transporters is specific for subcellular locations and involves interaction of transporters with specific cytoskeletal components, including actin (See Colour Plate 29)...

We have already seen in Section 2.2 how the transport of both anions and cations is a vital part of biochemistry. We will examine supramolecular models of biological ion channels in detail in Chapter 12 but here we focus on some simple ion transport systems (ionophores) relevant to simultaneous anion and cation binding. Because of the need to maintain overall and local charge neutrality during any transport process the transport of individual ions across a biological or artificial membrane never occurs in isolation. There are two kinds of primary transport processes. Ion exchange or antiport, occurs when chemically different ions of like charge such as Na+ and K+ are simultaneously transported in... 

Active transport of a molecule across a membrane against its concentration gradient requires an input of metabolic energy. In the case of ATP-driven active transport, the energy required for the transport of the molecule (Na+, K+, Ca2+ or H+) across the membrane is derived from the coupled hydrolysis of ATP (e.g Na+/K+-ATPase). In ion-driven active transport, the movement of the molecule to be transported across the membrane is coupled to the movement of an ion (either Na+ or H+) down its concentration gradient. If both the molecule to be transported and the ion move in the same direction across the membrane, the process is called symport (e.g. Na+/glucose transporter) if the molecule and the ion move in opposite directions it is called antiport (e.g. erythrocyte band 3 anion transporter). 

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